8z6w

Structure of EG.5.1 S trimer with 3 down-RBDs complex with antibody CYFN1006-2.

Method: ELECTRON MICROSCOPY Dmax: 202.8 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Spike glycoprotein,Fibritin,Expression Tag

synthetic construct

UniProt P0DTC2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 14–1208 Chain B; UniProt 14–1208 Chain C; UniProt 14–1208 Not recorded CYFN1006-2 light chain × 3 CYFN1006-2 heavy chain × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2152 other PDB entries and 2473 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 25–1215; UniProt 14–1208 Author chain B; PDBConstruct 25–1215; UniProt 14–1208 Author chain C; PDBConstruct 25–1215; UniProt 14–1208

Spike glycoprotein,Fibritin,Expression Tag

synthetic construct

UniProt P10104

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 458–485 Chain B; UniProt 458–485 Chain C; UniProt 458–485 Not recorded CYFN1006-2 light chain × 3 CYFN1006-2 heavy chain × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

104 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WAC_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1218–1245; UniProt 458–485 Author chain B; PDBConstruct 1218–1245; UniProt 458–485 Author chain C; PDBConstruct 1218–1245; UniProt 458–485

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8z6w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8z6w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8z6w
Deposition date deposition_date2024-04-19
Structure title titleStructure of EG.5.1 S trimer with 3 down-RBDs complex with antibody CYFN1006-2.
Keywords keywordsantibody, viral protein, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier60.53
Radius of gyration Rg (electron density) rg_electron60.64
Forward intensity I(0) i03422540000.00
Molecular weight molecular_weight495840.0 kDa
Excluded volume excluded_volume621560 ų
Envelope volume envelope_volume919820 ų
Hydration-shell volume shell_volume128440 ų
Envelope diameter envelope_diameter222.1
Shell Rg shell_rg60.25
Envelope Rg envelope_rg60.99
Shape Rg shape_rg60.64
Total Rg total_rg60.66
Total atoms total_atoms34950
Residues n_residues4521
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax202.8
Rg (real space) rg_real60.81
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real3.4220e+09
I(0) uncertainty (real space) i0_real_error6.9120e+07
Rg (reciprocal space) rg_reciprocal60.28
I(0) (reciprocal space) i0_reciprocal3420000000.0000
Solution quality estimate total_estimate0.8364
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.2
Skewness Skewness skewness0.550
Kurtosis Kurtosis kurtosis0.046
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha459600000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.449

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)